Celiac disease sufferers often endure a life of dietary restrictions, ensuring that no gluten, a product found in many commonly eaten foods, ever passes their lips.
But this may soon come to an end. Researchers in the Netherlands have found that an enzyme originally developed for commercial food processing -- AN-PEP -- may be able to break down gluten in the stomach before it reaches the small intestine. This information could be vital because the small intestine is where celiac disease originates.
According to the study's lead author, Frits Konig, professor of immunology at Leiden University Medical Center "There is a realistic chance that this enzyme can be used to develop an alternative treatment for celiac disease. It is very difficult to predict if such an enzyme-based treatment would actually be preferred over a gluten-free diet, but at the very least, it would provide patients with the option to occasionally follow a normal diet -- for example, when going out or during other social occasions, times when a gluten-free diet is certainly bothersome.
According to Konig about 1 percent of people in the United States and Europe are affected by celiac disease which is an autoimmune disease. It occurs when the body mistakes gluten molecules as foreign invaders to be destroyed. As a result parts of the small intestine are also destroyed along with the gluten moleculesduring the immune system response. This leads to a difficulty for the small intestine to properly absorb nutrients from food causing anemia and vitamin deficiencies. .
Therefore the only solution for avoiding the flare up of this disease would be to avoid gluten completely. However this is not an easy task. As Konig pointed out, "Gluten is a common protein found in wheat and related cereals like barley and rye. This means many common food products, like bread, breakfast cereals, pasta, cookies, etc., are forbidden. Moreover, gluten is often used as an additive in the food industry, so, many products that are not normally associated with wheat may contain gluten"..
As there is no animal model for celiac disease, treatments cannot be studied in animals. .
Konig said, "AN-PEP is very efficient and completely breaks down gluten proteins into fragments that are so small that they can no longer cause inflammation in the intestine. This we have also demonstrated by using white blood cells from patients that respond to gluten and cause inflammation in the intestine. These cells no longer respond to gluten when it has been treated with the AN-PEP enzyme"..
According to Konig AN-PEP is derived from Aspergillus niger, a common fungus. Since Aspergillus niger is already used in commercial food processing, he said side effects were unlikely from the treatment.
Konig said the next step is to conduct human trials.